Amontov S V, Tolosa E A, Goriachenkova E V
Biokhimiia. 1980 Nov;45(11):1960-3.
Covalent binding of the pyridoxal phosphate-dependent lyase--cystathionine-beta-synthase from chicken liver--by CNBr-activated Sepharose 4B and 6B resulted in catalytically active preparations of immobilized enzyme. Immobilized cystathionine-beta-synthase was shown to possess a higher stability as compared to the native enzyme. The maximum of activity of the obtained preparations was revealed at high temperatures (63 degrees), whereas the native enzyme had the temperature optimum at 40 degrees. The pH optimum of the enzyme activity was markedly shifted towards the alkaline region. The substrate specificity of the immobilized enzyme remained essentially unchanged.
用溴化氰活化的琼脂糖4B和6B将来自鸡肝的磷酸吡哆醛依赖性裂解酶——胱硫醚-β-合酶共价结合，得到了具有催化活性的固定化酶制剂。与天然酶相比，固定化胱硫醚-β-合酶显示出更高的稳定性。所得制剂的活性最大值出现在高温（63摄氏度）下，而天然酶的最适温度为40摄氏度。酶活性的最适pH值明显向碱性区域偏移。固定化酶的底物特异性基本保持不变。
